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Bioss
NARF Polyclonal Antibody
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Product Details
BS-11173R
Species Reactivity
Host/Isotype
Class
Type
Immunogen
Conjugate
Form
Concentration
Purification
Storage buffer
Contains
Storage conditions
Shipping conditions
Target Information
Several proteins have been found to be prenylated and methylated at their carboxyl-terminal ends. Prenylation was initially believed to be important only for membrane attachment. However, another role for prenylation appears to be its importance in protein-protein interactions. The only nuclear proteins known to be prenylated in mammalian cells are prelamin A- and B-type lamins. Prelamin A is farnesylated and carboxymethylated on the cysteine residue of a carboxyl-terminal CaaX motif. This post-translationally modified cysteine residue is removed from prelamin A when it is endoproteolytically processed into mature lamin A. The protein encoded by this gene binds to the prenylated prelamin A carboxyl-terminal tail domain. It may be a component of a prelamin A endoprotease complex. The encoded protein is located in the nucleus, where it partially colocalizes with the nuclear lamina. It shares limited sequence similarity with iron-only bacterial hydrogenases. Alternatively spliced transcript variants encoding different isoforms have been identified for this gene, including one with a novel exon that is generated by RNA editing.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
References (0)
Bioinformatics
Protein Aliases: IOP2; Iron-only hydrogenase-like protein 2; Nuclear prelamin A recognition factor; prenyl-dependent prelamin A binding protein
Gene Aliases: 4430402O11Rik; IOP2; NARF; RGD1310894
UniProt ID: (Human) Q9UHQ1, (Mouse) Q9CYQ7, (Rat) Q2YDU6
Entrez Gene ID: (Human) 26502, (Mouse) 67608, (Rat) 360681
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